STRINGSTRING
STRING protein interaction network
Nodes:
Network nodes represent proteins
splice isoforms or post-translational modifications are collapsed, i.e. each node represents all the proteins produced by a single, protein-coding gene locus.
Node Color
colored nodes:
query proteins and first shell of interactors
white nodes:
second shell of interactors
Node Content
empty nodes:
proteins of unknown 3D structure
filled nodes:
a 3D structure is known or predicted
Edges:
Edges represent protein-protein associations
associations are meant to be specific and meaningful, i.e. proteins jointly contribute to a shared function; this does not necessarily mean they are physically binding to each other.
Known Interactions
from curated databases
experimentally determined
Predicted Interactions
gene neighborhood
gene fusions
gene co-occurrence
Others
textmining
co-expression
protein homology
Your Input:
Neighborhood
Gene Fusion
Cooccurrence
Coexpression
Experiments
Databases
Textmining
[Homology]
Score
Afer_0100PFAM: Alpha/beta hydrolase fold-3 domain protein; KEGG: acr:Acry_0942 alpha/beta hydrolase domain- containing protein. (335 aa)    
Predicted Functional Partners:
nuoI
NADH-quinone oxidoreductase, chain I; NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be ubiquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient.
  
   0.883
Afer_0369
NADH-quinone oxidoreductase, chain G; NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient. Belongs to the complex I 75 kDa subunit family.
   
 
 0.877
Afer_0367
TIGRFAM: NADH-quinone oxidoreductase, E subunit; PFAM: NADH dehydrogenase (ubiquinone) 24 kDa subunit; KEGG: msm:MSMEG_2059 NADH-quinone oxidoreductase chain E.
    
   0.866
Afer_1826
PFAM: Rieske [2Fe-2S] domain protein; KEGG: fal:FRAAL5110 ubiquinol-cytochrome c reductase iron-sulfur subunit (Rieske iron-sulfur protein).
   
   0.850
Afer_0368
PFAM: Respiratory-chain NADH dehydrogenase domain 51 kDa subunit; KEGG: mxa:MXAN_1085 NADH dehydrogenase I, F subunit.
    
   0.846
Afer_0998
PFAM: Respiratory-chain NADH dehydrogenase domain 51 kDa subunit; KEGG: sco:SCP1.160c putative oxidoreductase.
    
   0.846
acpP
Acyl carrier protein; Carrier of the growing fatty acid chain in fatty acid biosynthesis.
   
 
 0.803
acpP-2
Phosphopantetheine-binding; Carrier of the growing fatty acid chain in fatty acid biosynthesis; Belongs to the acyl carrier protein (ACP) family.
   
 
 0.803
nuoA
NADH-ubiquinone/plastoquinone oxidoreductase chain 3; NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be a menaquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient; Belongs to the complex I subunit 3 family.
    
   0.778
Afer_1377
PFAM: ferredoxin; Oxidoreductase FAD-binding domain protein; oxidoreductase FAD/NAD(P)-binding domain protein; KEGG: dar:Daro_0368 ferredoxin:oxidoreductase FAD/NAD(P)-binding:oxidoreductase FAD-binding region.
    
 
 0.778
Your Current Organism:
Acidimicrobium ferrooxidans
NCBI taxonomy Id: 525909
Other names: A. ferrooxidans DSM 10331, Acidimicrobium ferrooxidans DSM 10331, Acidimicrobium ferrooxidans ICP, Acidimicrobium ferrooxidans str. DSM 10331, Acidimicrobium ferrooxidans strain DSM 10331
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